ID   PUR1_STAAN              Reviewed;         494 AA.
AC   P99164; Q99V27;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   27-MAR-2024, entry version 118.
DE   RecName: Full=Amidophosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01931};
DE            Short=ATase {ECO:0000255|HAMAP-Rule:MF_01931};
DE            EC=2.4.2.14 {ECO:0000255|HAMAP-Rule:MF_01931};
DE   AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_01931};
DE            Short=GPATase {ECO:0000255|HAMAP-Rule:MF_01931};
DE   Flags: Precursor;
GN   Name=purF {ECO:0000255|HAMAP-Rule:MF_01931}; OrderedLocusNames=SA0922;
OS   Staphylococcus aureus (strain N315).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=158879;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=N315;
RX   PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA   Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA   Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA   Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA   Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA   Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA   Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA   Hiramatsu K.;
RT   "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL   Lancet 357:1225-1240(2001).
RN   [2]
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=N315;
RX   PubMed=15590099; DOI=10.1016/j.mimet.2004.09.017;
RA   Scherl A., Francois P., Bento M., Deshusses J.M., Charbonnier Y.,
RA   Converset V., Huyghe A., Walter N., Hoogland C., Appel R.D., Sanchez J.-C.,
RA   Zimmermann-Ivol C.G., Corthals G.L., Hochstrasser D.F., Schrenzel J.;
RT   "Correlation of proteomic and transcriptomic profiles of Staphylococcus
RT   aureus during the post-exponential phase of growth.";
RL   J. Microbiol. Methods 60:247-257(2005).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   STRAIN=N315;
RA   Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT   "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT   aureus strain N315.";
RL   Submitted (OCT-2007) to UniProtKB.
CC   -!- FUNCTION: Catalyzes the formation of phosphoribosylamine from
CC       phosphoribosylpyrophosphate (PRPP) and glutamine. {ECO:0000255|HAMAP-
CC       Rule:MF_01931}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=5-phospho-beta-D-ribosylamine + diphosphate + L-glutamate = 5-
CC         phospho-alpha-D-ribose 1-diphosphate + H2O + L-glutamine;
CC         Xref=Rhea:RHEA:14905, ChEBI:CHEBI:15377, ChEBI:CHEBI:29985,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:58017, ChEBI:CHEBI:58359,
CC         ChEBI:CHEBI:58681; EC=2.4.2.14; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01931};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01931};
CC       Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP-Rule:MF_01931};
CC   -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-
CC       (5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-
CC       diphosphate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_01931}.
CC   -!- SIMILARITY: In the C-terminal section; belongs to the purine/pyrimidine
CC       phosphoribosyltransferase family. {ECO:0000255|HAMAP-Rule:MF_01931}.
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DR   EMBL; BA000018; BAB42167.1; -; Genomic_DNA.
DR   PIR; D89876; D89876.
DR   RefSeq; WP_000483720.1; NC_002745.2.
DR   AlphaFoldDB; P99164; -.
DR   SMR; P99164; -.
DR   MEROPS; C44.001; -.
DR   EnsemblBacteria; BAB42167; BAB42167; BAB42167.
DR   KEGG; sau:SA0922; -.
DR   HOGENOM; CLU_022389_3_1_9; -.
DR   UniPathway; UPA00074; UER00124.
DR   Proteomes; UP000000751; Chromosome.
DR   GO; GO:0004044; F:amidophosphoribosyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro.
DR   CDD; cd00715; GPATase_N; 1.
DR   CDD; cd06223; PRTases_typeI; 1.
DR   Gene3D; 3.40.50.2020; -; 1.
DR   Gene3D; 3.60.20.10; Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1; 1.
DR   HAMAP; MF_01931; PurF; 1.
DR   InterPro; IPR017932; GATase_2_dom.
DR   InterPro; IPR029055; Ntn_hydrolases_N.
DR   InterPro; IPR000836; PRibTrfase_dom.
DR   InterPro; IPR029057; PRTase-like.
DR   InterPro; IPR005854; PurF.
DR   InterPro; IPR035584; PurF_N.
DR   NCBIfam; TIGR01134; purF; 1.
DR   PANTHER; PTHR11907; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1.
DR   PANTHER; PTHR11907:SF0; AMIDOPHOSPHORIBOSYLTRANSFERASE; 1.
DR   Pfam; PF13537; GATase_7; 1.
DR   Pfam; PF00156; Pribosyltran; 1.
DR   PIRSF; PIRSF000485; Amd_phspho_trans; 1.
DR   SUPFAM; SSF56235; N-terminal nucleophile aminohydrolases (Ntn hydrolases); 1.
DR   SUPFAM; SSF53271; PRTase-like; 1.
DR   PROSITE; PS51278; GATASE_TYPE_2; 1.
DR   PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1.
DR   SWISS-2DPAGE; P99164; -.
PE   1: Evidence at protein level;
KW   Glutamine amidotransferase; Glycosyltransferase; Magnesium; Metal-binding;
KW   Purine biosynthesis; Transferase.
FT   PROPEP          1..10
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000029265"
FT   CHAIN           11..494
FT                   /note="Amidophosphoribosyltransferase"
FT                   /id="PRO_0000029266"
FT   DOMAIN          11..231
FT                   /note="Glutamine amidotransferase type-2"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT   ACT_SITE        11
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT   BINDING         294
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT   BINDING         356
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
FT   BINDING         357
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01931"
SQ   SEQUENCE   494 AA;  54383 MW;  CCF5D947C381646D CRC64;
     MFNYSGLNEE CGVFGIWNHP EAAQLTYMGL HSLQHRGQEG AGIVVSDQNE LKGERGLGLL
     TEAINDDQME RLKGYQHAIG HVRYATSGNK GIENIQPFLY HFYDMSVGIC HNGNLINAKS
     LRQNLEKQGA IFHSSSDTEV IMHLIRRSKA PTFEEALKES LRKVKGGFTF AILTKDALYG
     AVDPNAIRPL VVGKMKDGTY ILASETCAID VLGAEFVQDI HAGEYVVIND KGITVKSYTH
     HTTTAISAME YIYFARPDST IAGKNVHAVR KASGKKLAQE SPVNADMVIG VPNSSLSAAS
     GYAEEIGLPY EMGLVKNQYV ARTFIQPTQE LREQGVRVKL SAVKDIVDGK NIILVDDSIV
     RGTTIRRIVK MLKDSGANKV HVRIASPEFM FPSFYGIDVS TTAELISASK SPEEIKDYIG
     ADSLAYLSVD GLIESIGLDY DAPYSGLCVE SFTGDYPAGL YDYEANYKAH LSHRQKQYIS
     KNKHFFDSEG NLNV
//